Research@StAndrews
 
The University of St Andrews

Research@StAndrews:FullText >
University of St Andrews Research >
University of St Andrews Research >
University of St Andrews Research >

Please use this identifier to cite or link to this item: http://hdl.handle.net/10023/1147
This item has been viewed 4 times in the last year. View Statistics

Files in This Item:

File Description SizeFormat
ElliottGeneralVirology90-FunctionalAnalysis.pdf806.21 kBAdobe PDFView/Open
Title: Functional analysis of the Bunyamwera orthobunyavirus Gc glycoprotein
Authors: Shi, Xiaohong
Goli, Josthna
Clark, Gordon
Brauburger, Kristina
Elliott, Richard Michael
Keywords: La-crosse virus
California encephalitis-virus
Nonstructural protein NSM
Membrane-fusion
Cell-fusion
Intracellular trafficking
Tissue-culture
Lacrosse virus
M RNA
G1
QR Microbiology
Issue Date: Oct-2009
Citation: Shi , X , Goli , J , Clark , G , Brauburger , K & Elliott , R M 2009 , ' Functional analysis of the Bunyamwera orthobunyavirus Gc glycoprotein ' Journal of General Virology , vol 90 , no. 10 , pp. 2483-2492 .
Abstract: The virion glycoproteins Gn and Gc of Bunyamwera orthobunyavirus (BUNV, family Bunyaviridae) are encoded by the M RNA genome segment and have roles in both viral attachment and membrane fusion. To investigate further the structure and function of the Gc protein in viral replication we generated twelve mutants that contain truncations from the N-terminus. The effects of these deletions were analysed with regard to Golgi targeting, low-pH dependent membrane fusion, infectious virus-like particle (VLP) formation and virus infectivity. Our results showed that the N-terminal half (453 residues) of the Gc ectodomain (909 residues in total) is dispensable for Golgi trafficking and cell fusion. However, deletions in this region resulted in significant reduction in VLP formation. Four mutant viruses that contain N-terminal deletions in their Gc proteins were rescued, and found to be attenuated to different degrees in BHK-21 cells. Taken together, our data indicate that the N-terminal half of the Gc ectodomain is dispensable for replication in cell culture, whereas the C-terminal half is required to mediate cell fusion. A model for the domain structure of the Gc ectodomain is proposed.
Version: Publisher PDF
Status: Peer reviewed
URI: http://hdl.handle.net/10023/1147
DOI: http://dx.doi.org/10.1099/vir.0.013540-0
ISSN: 0022-1317
Type: Journal article
Rights: This article is published by the Society for General Microbiology under the Open Option which allows reuse for non commercial purposes.
Appears in Collections:University of St Andrews Research
Biology Research
Biomedical Sciences Research Complex (BSRC) Research



This item is protected by original copyright

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

 

DSpace Software Copyright © 2002-2012  Duraspace - Feedback
For help contact: Digital-Repository@st-andrews.ac.uk | Copyright for this page belongs to St Andrews University Library | Terms and Conditions (Cookies)